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Yorodumi- PDB-2kse: Backbone structure of the membrane domain of E. coli histidine ki... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2kse | ||||||
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Title | Backbone structure of the membrane domain of E. coli histidine kinase receptor QseC, Center for Structures of Membrane Proteins (CSMP) target 4311C | ||||||
Components | Sensor protein qseC | ||||||
Keywords | TRANSFERASE / methods development / Histidine kinase receptor / membrane domain / two-helical hairpin / cell-free synthesis / ATP-binding / Cell inner membrane / Cell membrane / Kinase / Membrane / Nucleotide-binding / Phosphoprotein / Transmembrane / Two-component regulatory system / Structural Genomics / PSI-2 / Protein Structure Initiative / Center for Structures of Membrane Proteins / CSMP | ||||||
Function / homology | Function and homology information regulation of cell motility / histidine kinase / phosphorelay signal transduction system / phosphorelay sensor kinase activity / small molecule binding / ATP binding / plasma membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Maslennikov, I. / Klammt, C. / Kefala, G. / Esquivies, L. / Kwiatkowski, W. / Choe, S. / Center for Structures of Membrane Proteins (CSMP) | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2010 Title: Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis. Authors: Maslennikov, I. / Klammt, C. / Hwang, E. / Kefala, G. / Okamura, M. / Esquivies, L. / Mors, K. / Glaubitz, C. / Kwiatkowski, W. / Jeon, Y.H. / Choe, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kse.cif.gz | 525 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kse.ent.gz | 426.3 KB | Display | PDB format |
PDBx/mmJSON format | 2kse.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2kse_validation.pdf.gz | 347.4 KB | Display | wwPDB validaton report |
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Full document | 2kse_full_validation.pdf.gz | 536.5 KB | Display | |
Data in XML | 2kse_validation.xml.gz | 25.4 KB | Display | |
Data in CIF | 2kse_validation.cif.gz | 41.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ks/2kse ftp://data.pdbj.org/pub/pdb/validation_reports/ks/2kse | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 21343.533 Da / Num. of mol.: 1 / Fragment: sequence database residues 2-185 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: b3026, JW2994, qseC, ygiY / Production host: CELL-FREE SYNTHESIS (others) / References: UniProt: P40719, histidine kinase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.5 mM DSS, 20 mM Mes-BisTris, 100 mM 1-myristoyl-2-hydroxy-sn-glycero-3-[phospho-rac-(1-glycerol)], 0.3 mM [U-99% 13C; U-99% 15N] Protein, 95% H2O/5% D2O Solvent system: 95% H2O/5% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | pH: 6.0 / Pressure: ambient / Temperature: 313 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, simulated annealing / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |